Adducin alpha (C-Term) antibody

Antigen: Adducin alpha

Binding Site: C-Term

Clonality: Monoclonal

Host: Rabbit

Reactivity: Human

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC)

Certificates: ISO 9001:2008

Catalog no.: ABIN649254

Additional Information

Gene ID: 118

UniProt: P35611

Description: Other names: ADD1, ADDA, Alpha-adducin, Erythrocyte adducin subunit alpha

Characteristics: Rabbit Monoclonal Antibody

Specificity: A synthetic peptide corresponding to residues in the C-term of human Adducin was used as immunogen.

Molecular Weight: 130 kDA

Comments:

Background: Adducin is a membrane skeletal protein that binds to actin filaments (F-actin) and promotes the association of spectrin with F-actin to form a spectrin-actin meshwork beneath plasma membranes (1-2). Adducin is a heterodimeric protein that consists of related subunits, α, and β,, or α, and γ, subunits (3). Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinase C (PKC), and protein kinase A (PKA) (4). Phosphorylation of adducing alpha by Rho-kinase at Thr445 and Thr480 enhances the F-actin-binding activity of adducing alpha (5).

Application Details

Application Notes: The suggested dilution is: WB: ~~ 1:500~1000 ICC: ~~ 1:250~500 IHC: ~~ 1:250~500

Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Storage: Adducin alpha Antibody (C-term) can be stored at -20°C for up to 12 months from time of receipt.

Research Area: Signaling, Phospho-specific antibodies, Protein Modifications, Cell Structure

Restrictions: For Research Use only

Publications

Product: Ling, Gardner, Bennett: "Protein kinase C phosphorylates a recently identified membrane skeleton-associated calmodulin-binding protein in human erythrocytes." in: The Journal of biological chemistry, Vol. 261, Issue 30, pp. 13875-8, 1986 (PubMed).

Dong, Chapline, Mousseau et al.: "35H, a sequence isolated as a protein kinase C binding protein, is a novel member of the adducin family." in: The Journal of biological chemistry, Vol. 270, Issue 43, pp. 25534-40, 1995 (PubMed).

Kuhlman, Hughes, Bennett et al.: "A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments." in: The Journal of biological chemistry, Vol. 271, Issue 14, pp. 7986-91, 1996 (PubMed).